The development of a tag-switch technique allows for selective labeling of protein S-sulfhydrated residues, advancing the study of H2S-mediated signaling pathways.
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Tag-switch labeling aids S-sulfhydration studies in animal models; leaves open translation to human cardiovascular H2S signaling.
Protein S-sulfhydration (forming -S-SH adducts from cysteine residues) is a newly defined oxidative posttranslational modification and plays an important role in H2 S-mediated signaling pathways. In this study we report the first selective, "tag-switch" method which can directly label protein S-sulfhydrated residues by forming stable thioether conjugates. Furthermore we demonstrate that H2 S alone cannot lead to S-sulfhydration and that the two possible physiological mechanisms include reaction with protein sulfenic acids (P-SOH) or the involvement of metal centers which would facilitate the oxidation of H2 S to HS(.) .
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Zhang et al. (2013) studied this question.
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